Format

Send to

Choose Destination
See comment in PubMed Commons below
Structure. 2010 May 12;18(5):584-93. doi: 10.1016/j.str.2010.02.015.

The Prp19 WD40 domain contains a conserved protein interaction region essential for its function.

Author information

1
Department of Biochemistry, Vanderbilt University, Nashville, TN 37232, USA. craig.vanderkooi@uky.edu

Abstract

Prp19 is a member of the WD40 repeat family of E3 ubiquitin ligases and a conserved eukaryotic RNA splicing factor essential for activation and stabilization of the spliceosome. To understand the role of the WD40 repeat domain of Prp19 we have determined its structure using X-ray crystallography. The domain has a distorted seven bladed WD40 architecture with significant asymmetry due to irregular packing of blades one and seven into the core of the WD40 domain. Structure-based mutagenesis identified a highly conserved surface centered around blade five that is required for the physical interaction between Prp19 and Cwc2, another essential splicing factor. This region is found to be required for Prp19 function and yeast viability. Experiments in vitro and in vivo demonstrate that two molecules of Cwc2 bind to the Prp19 tetramer. These coupled structural and functional studies provide a model for the functional architecture of Prp19.

PMID:
20462492
PMCID:
PMC2871033
DOI:
10.1016/j.str.2010.02.015
[Indexed for MEDLINE]
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Elsevier Science Icon for PubMed Central
    Loading ...
    Support Center